data_2959 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 2959 _Entry.Title ; High-resolution Three-Dimensional Structure of Reduced Recombinant Human Thioredoxin in Solution ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1995-07-31 _Entry.Accession_date 1996-04-13 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination BMRB _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Julie Forman-Kay . D. . 2959 2 G. Clore . Marius . 2959 3 Paul Wingfield . . . 2959 4 Angela Gronenborn . M. . 2959 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 2959 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 9 2959 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 5 . . 2010-06-17 . revision BMRB 'Complete natural source information' 2959 4 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 2959 3 . . 1996-04-13 . revision BMRB 'Link to the Protein Data Bank added' 2959 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 2959 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 2959 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 2959 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Forman-Kay, Julie D., Clore, G. Marius, Wingfield, Paul, Gronenborn, Angela M., "High-resolution Three-Dimensional Structure of Reduced Recombinant Human Thioredoxin in Solution," Biochemistry 30, 2685-2698 (1991). ; _Citation.Title ; High-resolution Three-Dimensional Structure of Reduced Recombinant Human Thioredoxin in Solution ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 30 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 2685 _Citation.Page_last 2698 _Citation.Year 1991 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Julie Forman-Kay . D. . 2959 1 2 G. Clore . Marius . 2959 1 3 Paul Wingfield . . . 2959 1 4 Angela Gronenborn . M. . 2959 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_thioredoxin _Assembly.Sf_category assembly _Assembly.Sf_framecode system_thioredoxin _Assembly.Entry_ID 2959 _Assembly.ID 1 _Assembly.Name thioredoxin _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic . _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 thioredoxin 1 $thioredoxin . . . . . . . . . 2959 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1AIU . 'Human Thioredoxin (D60n Mutant, Reduced Form)' . . . . 2959 1 yes PDB 1AUC . 'Human Thioredoxin (Oxidized With Diamide)' . . . . 2959 1 yes PDB 1ERT . 'Human Thioredoxin (Reduced Form)' . . . . 2959 1 yes PDB 1ERU . 'Human Thioredoxin (Oxidized Form)' . . . . 2959 1 yes PDB 1ERV . 'Human Thioredoxin Mutant With Cys 73 Replaced By Ser (Reduced Form)' . . . . 2959 1 yes PDB 3TRX . 'Thioredoxin (Reduced Form)' . . . . 2959 1 yes PDB 4TRX . 'Thioredoxin (Reduced Form)' . . . . 2959 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID thioredoxin system 2959 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_thioredoxin _Entity.Sf_category entity _Entity.Sf_framecode thioredoxin _Entity.Entry_ID 2959 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name thioredoxin _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can ; VKQIESKTAFQEALDAAGDK LVVVDFSATWCGPCKMIKPF FHSLSEKYSNVIFLEVDVDD CQDVASECEVKCTPTFQFFK KGQKVGEFSGANKEKLEATI NELV ; _Entity.Polymer_seq_one_letter_code ; VKQIESKTAFQEALDAAGDK LVVVDFSATWCGPCKMIKPF FHSLSEKYSNVIFLEVDVDD CQDVASECEVKCTPTFQFFK KGQKVGEFSGANKEKLEATI NELV ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 104 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 1400 . thioredoxin . . . . . 100.00 104 100.00 100.00 1.06e-67 . . . . 2959 1 2 no BMRB 253 . thioredoxin . . . . . 100.00 105 100.00 100.00 9.63e-68 . . . . 2959 1 3 no BMRB 254 . thioredoxin . . . . . 100.00 104 100.00 100.00 1.06e-67 . . . . 2959 1 4 no BMRB 255 . thioredoxin . . . . . 100.00 104 100.00 100.00 1.06e-67 . . . . 2959 1 5 no BMRB 256 . thioredoxin . . . . . 100.00 104 100.00 100.00 1.06e-67 . . . . 2959 1 6 no BMRB 257 . thioredoxin . . . . . 100.00 105 100.00 100.00 9.63e-68 . . . . 2959 1 7 no BMRB 283 . thioredoxin . . . . . 100.00 105 100.00 100.00 9.63e-68 . . . . 2959 1 8 no BMRB 284 . thioredoxin . . . . . 100.00 104 100.00 100.00 1.06e-67 . . . . 2959 1 9 no BMRB 2958 . thioredoxin . . . . . 100.00 105 100.00 100.00 9.63e-68 . . . . 2959 1 10 no PDB 1AIU . "Human Thioredoxin (D60n Mutant, Reduced Form)" . . . . . 100.00 105 98.08 99.04 1.83e-66 . . . . 2959 1 11 no PDB 1AUC . "Human Thioredoxin (Oxidized With Diamide)" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 2959 1 12 no PDB 1ERT . "Human Thioredoxin (Reduced Form)" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 2959 1 13 no PDB 1ERU . "Human Thioredoxin (Oxidized Form)" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 2959 1 14 no PDB 1ERV . "Human Thioredoxin Mutant With Cys 73 Replaced By Ser (Reduced Form)" . . . . . 100.00 105 98.08 98.08 6.49e-66 . . . . 2959 1 15 no PDB 1ERW . "Human Thioredoxin Double Mutant With Cys 32 Replaced By Ser And Cys 35 Replaced By Ser" . . . . . 100.00 105 97.12 97.12 5.32e-65 . . . . 2959 1 16 no PDB 1TRS . "The High-Resolution Three-Dimensional Solution Structures Of The Oxidized And Reduced States Of Human Thioredoxin" . . . . . 100.00 105 97.12 97.12 2.99e-65 . . . . 2959 1 17 no PDB 1TRU . "The High-Resolution Three-Dimensional Solution Structures Of The Oxidized And Reduced States Of Human Thioredoxin" . . . . . 100.00 105 97.12 97.12 2.99e-65 . . . . 2959 1 18 no PDB 1TRV . "The High-resolution Three-dimensional Solution Structures Of The Oxidized And Reduced States Of Human Thioredoxin" . . . . . 100.00 105 97.12 97.12 2.99e-65 . . . . 2959 1 19 no PDB 1TRW . "The High-Resolution Three-Dimensional Solution Structures Of The Oxidized And Reduced States Of Human Thioredoxin" . . . . . 100.00 105 97.12 97.12 2.99e-65 . . . . 2959 1 20 no PDB 2HSH . "Crystal Structure Of C73s Mutant Of Human Thioredoxin-1 Oxidized With H2o2" . . . . . 100.00 105 98.08 98.08 6.49e-66 . . . . 2959 1 21 no PDB 2HXK . "Crystal Structure Of S-Nitroso Thioredoxin" . . . . . 100.00 105 97.12 97.12 1.48e-64 . . . . 2959 1 22 no PDB 2IFQ . "Crystal Structure Of S-Nitroso Thioredoxin" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 2959 1 23 no PDB 2IIY . "Crystal Structure Of S-Nitroso Thioredoxin" . . . . . 100.00 105 97.12 97.12 1.48e-64 . . . . 2959 1 24 no PDB 3E3E . "Human Thioredoxin Double Mutant C35s,C73r" . . . . . 100.00 105 97.12 97.12 9.70e-65 . . . . 2959 1 25 no PDB 3M9J . "Crystal Structure Of Human Thioredoxin C6973S DOUBLE MUTANT, REDUCED Form" . . . . . 100.00 105 97.12 97.12 5.32e-65 . . . . 2959 1 26 no PDB 3M9K . "Crystal Structure Of Human Thioredoxin C6973S DOUBLE-Mutant, Oxidized Form" . . . . . 100.00 105 97.12 97.12 5.32e-65 . . . . 2959 1 27 no PDB 3QFA . "Crystal Structure Of The Human Thioredoxin Reductase-Thioredoxin Complex" . . . . . 100.00 116 97.12 97.12 2.05e-65 . . . . 2959 1 28 no PDB 3QFB . "Crystal Structure Of The Human Thioredoxin Reductase-Thioredoxin Complex" . . . . . 100.00 116 97.12 97.12 2.05e-65 . . . . 2959 1 29 no PDB 3TRX . "High-Resolution Three-Dimensional Structure Of Reduced Recombinant Human Thioredoxin In Solution" . . . . . 100.00 105 100.00 100.00 9.63e-68 . . . . 2959 1 30 no PDB 4LL1 . "The Structure Of The Trx And Txnip Complex" . . . . . 100.00 105 98.08 98.08 5.27e-66 . . . . 2959 1 31 no PDB 4LL4 . "The Structure Of The Trx And Txnip Complex" . . . . . 100.00 105 98.08 98.08 5.27e-66 . . . . 2959 1 32 no PDB 4PUF . "Complex Between The Salmonella T3ss Effector Slrp And Its Human Target Thioredoxin-1" . . . . . 100.00 117 99.04 99.04 2.29e-67 . . . . 2959 1 33 no PDB 4TRX . "High-Resolution Three-Dimensional Structure Of Reduced Recombinant Human Thioredoxin In Solution" . . . . . 100.00 105 100.00 100.00 9.63e-68 . . . . 2959 1 34 no DBJ BAF82197 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 2959 1 35 no EMBL CAA38410 . "thioredoxin [Homo sapiens]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 2959 1 36 no EMBL CAA54687 . "ATL-derived factor/thioredoxin [Homo sapiens]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 2959 1 37 no EMBL CAG28593 . "TXN [Homo sapiens]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 2959 1 38 no EMBL CAH91537 . "hypothetical protein [Pongo abelii]" . . . . . 100.96 106 98.10 98.10 4.09e-65 . . . . 2959 1 39 no EMBL CEK46668 . "Thioredoxin-1 [synthetic construct]" . . . . . 100.00 125 99.04 99.04 1.58e-67 . . . . 2959 1 40 no GB AAA74596 . "thioredoxin [Homo sapiens]" . . . . . 100.00 105 99.04 99.04 4.07e-67 . . . . 2959 1 41 no GB AAF86466 . "thioredoxin 1 [Homo sapiens]" . . . . . 100.00 105 99.04 99.04 4.07e-67 . . . . 2959 1 42 no GB AAF87085 . "thioredoxin [Homo sapiens]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 2959 1 43 no GB AAG34699 . "thioredoxin [Homo sapiens]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 2959 1 44 no GB AAH03377 . "Thioredoxin [Homo sapiens]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 2959 1 45 no REF NP_001125903 . "thioredoxin [Pongo abelii]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 2959 1 46 no REF NP_003320 . "thioredoxin isoform 1 [Homo sapiens]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 2959 1 47 no REF WP_052431332 . "hypothetical protein, partial [Acinetobacter sp. MII]" . . . . . 97.12 101 99.01 99.01 4.76e-65 . . . . 2959 1 48 no REF XP_001142154 . "PREDICTED: thioredoxin [Pan troglodytes]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 2959 1 49 no REF XP_003257823 . "PREDICTED: thioredoxin [Nomascus leucogenys]" . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 2959 1 50 no SP P10599 . "RecName: Full=Thioredoxin; Short=Trx; AltName: Full=ATL-derived factor; Short=ADF; AltName: Full=Surface-associated sulphydryl " . . . . . 100.00 105 99.04 99.04 5.34e-67 . . . . 2959 1 51 no SP Q5R9M3 . "RecName: Full=Thioredoxin; Short=Trx" . . . . . 100.96 106 98.10 98.10 4.09e-65 . . . . 2959 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'N-val form' variant 2959 1 thioredoxin common 2959 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . VAL . 2959 1 2 . LYS . 2959 1 3 . GLN . 2959 1 4 . ILE . 2959 1 5 . GLU . 2959 1 6 . SER . 2959 1 7 . LYS . 2959 1 8 . THR . 2959 1 9 . ALA . 2959 1 10 . PHE . 2959 1 11 . GLN . 2959 1 12 . GLU . 2959 1 13 . ALA . 2959 1 14 . LEU . 2959 1 15 . ASP . 2959 1 16 . ALA . 2959 1 17 . ALA . 2959 1 18 . GLY . 2959 1 19 . ASP . 2959 1 20 . LYS . 2959 1 21 . LEU . 2959 1 22 . VAL . 2959 1 23 . VAL . 2959 1 24 . VAL . 2959 1 25 . ASP . 2959 1 26 . PHE . 2959 1 27 . SER . 2959 1 28 . ALA . 2959 1 29 . THR . 2959 1 30 . TRP . 2959 1 31 . CYS . 2959 1 32 . GLY . 2959 1 33 . PRO . 2959 1 34 . CYS . 2959 1 35 . LYS . 2959 1 36 . MET . 2959 1 37 . ILE . 2959 1 38 . LYS . 2959 1 39 . PRO . 2959 1 40 . PHE . 2959 1 41 . PHE . 2959 1 42 . HIS . 2959 1 43 . SER . 2959 1 44 . LEU . 2959 1 45 . SER . 2959 1 46 . GLU . 2959 1 47 . LYS . 2959 1 48 . TYR . 2959 1 49 . SER . 2959 1 50 . ASN . 2959 1 51 . VAL . 2959 1 52 . ILE . 2959 1 53 . PHE . 2959 1 54 . LEU . 2959 1 55 . GLU . 2959 1 56 . VAL . 2959 1 57 . ASP . 2959 1 58 . VAL . 2959 1 59 . ASP . 2959 1 60 . ASP . 2959 1 61 . CYS . 2959 1 62 . GLN . 2959 1 63 . ASP . 2959 1 64 . VAL . 2959 1 65 . ALA . 2959 1 66 . SER . 2959 1 67 . GLU . 2959 1 68 . CYS . 2959 1 69 . GLU . 2959 1 70 . VAL . 2959 1 71 . LYS . 2959 1 72 . CYS . 2959 1 73 . THR . 2959 1 74 . PRO . 2959 1 75 . THR . 2959 1 76 . PHE . 2959 1 77 . GLN . 2959 1 78 . PHE . 2959 1 79 . PHE . 2959 1 80 . LYS . 2959 1 81 . LYS . 2959 1 82 . GLY . 2959 1 83 . GLN . 2959 1 84 . LYS . 2959 1 85 . VAL . 2959 1 86 . GLY . 2959 1 87 . GLU . 2959 1 88 . PHE . 2959 1 89 . SER . 2959 1 90 . GLY . 2959 1 91 . ALA . 2959 1 92 . ASN . 2959 1 93 . LYS . 2959 1 94 . GLU . 2959 1 95 . LYS . 2959 1 96 . LEU . 2959 1 97 . GLU . 2959 1 98 . ALA . 2959 1 99 . THR . 2959 1 100 . ILE . 2959 1 101 . ASN . 2959 1 102 . GLU . 2959 1 103 . LEU . 2959 1 104 . VAL . 2959 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . VAL 1 1 2959 1 . LYS 2 2 2959 1 . GLN 3 3 2959 1 . ILE 4 4 2959 1 . GLU 5 5 2959 1 . SER 6 6 2959 1 . LYS 7 7 2959 1 . THR 8 8 2959 1 . ALA 9 9 2959 1 . PHE 10 10 2959 1 . GLN 11 11 2959 1 . GLU 12 12 2959 1 . ALA 13 13 2959 1 . LEU 14 14 2959 1 . ASP 15 15 2959 1 . ALA 16 16 2959 1 . ALA 17 17 2959 1 . GLY 18 18 2959 1 . ASP 19 19 2959 1 . LYS 20 20 2959 1 . LEU 21 21 2959 1 . VAL 22 22 2959 1 . VAL 23 23 2959 1 . VAL 24 24 2959 1 . ASP 25 25 2959 1 . PHE 26 26 2959 1 . SER 27 27 2959 1 . ALA 28 28 2959 1 . THR 29 29 2959 1 . TRP 30 30 2959 1 . CYS 31 31 2959 1 . GLY 32 32 2959 1 . PRO 33 33 2959 1 . CYS 34 34 2959 1 . LYS 35 35 2959 1 . MET 36 36 2959 1 . ILE 37 37 2959 1 . LYS 38 38 2959 1 . PRO 39 39 2959 1 . PHE 40 40 2959 1 . PHE 41 41 2959 1 . HIS 42 42 2959 1 . SER 43 43 2959 1 . LEU 44 44 2959 1 . SER 45 45 2959 1 . GLU 46 46 2959 1 . LYS 47 47 2959 1 . TYR 48 48 2959 1 . SER 49 49 2959 1 . ASN 50 50 2959 1 . VAL 51 51 2959 1 . ILE 52 52 2959 1 . PHE 53 53 2959 1 . LEU 54 54 2959 1 . GLU 55 55 2959 1 . VAL 56 56 2959 1 . ASP 57 57 2959 1 . VAL 58 58 2959 1 . ASP 59 59 2959 1 . ASP 60 60 2959 1 . CYS 61 61 2959 1 . GLN 62 62 2959 1 . ASP 63 63 2959 1 . VAL 64 64 2959 1 . ALA 65 65 2959 1 . SER 66 66 2959 1 . GLU 67 67 2959 1 . CYS 68 68 2959 1 . GLU 69 69 2959 1 . VAL 70 70 2959 1 . LYS 71 71 2959 1 . CYS 72 72 2959 1 . THR 73 73 2959 1 . PRO 74 74 2959 1 . THR 75 75 2959 1 . PHE 76 76 2959 1 . GLN 77 77 2959 1 . PHE 78 78 2959 1 . PHE 79 79 2959 1 . LYS 80 80 2959 1 . LYS 81 81 2959 1 . GLY 82 82 2959 1 . GLN 83 83 2959 1 . LYS 84 84 2959 1 . VAL 85 85 2959 1 . GLY 86 86 2959 1 . GLU 87 87 2959 1 . PHE 88 88 2959 1 . SER 89 89 2959 1 . GLY 90 90 2959 1 . ALA 91 91 2959 1 . ASN 92 92 2959 1 . LYS 93 93 2959 1 . GLU 94 94 2959 1 . LYS 95 95 2959 1 . LEU 96 96 2959 1 . GLU 97 97 2959 1 . ALA 98 98 2959 1 . THR 99 99 2959 1 . ILE 100 100 2959 1 . ASN 101 101 2959 1 . GLU 102 102 2959 1 . LEU 103 103 2959 1 . VAL 104 104 2959 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 2959 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $thioredoxin . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 2959 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 2959 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $thioredoxin . 'not available' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 2959 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 2959 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_condition_set_one _Sample_condition_list.Entry_ID 2959 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 5.5 . na 2959 1 temperature 313 . K 2959 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 2959 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 2959 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 unknown unknown . 0 'spectrometer information not available' . . 2959 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 2959 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 . . . . . . . . . . . . 1 $sample_one . . . 1 $sample_condition_set_one . . . 1 $spectrometer_list . . . . . . . . . . . . . . . . 2959 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_par_set_one _Chem_shift_reference.Entry_ID 2959 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H . DSS . . . . . ppm 0 . . . . . . 1 $entry_citation . . 1 $entry_citation 2959 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_data_set_one _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode 'chemical_shift_assignment_data_set_one' _Assigned_chem_shift_list.Entry_ID 2959 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_condition_set_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_par_set_one _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_one . 2959 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 38 38 LYS HA H 1 4.33 . . 1 . . . . . . . . 2959 1 2 . 1 1 38 38 LYS HB2 H 1 2.17 . . 2 . . . . . . . . 2959 1 3 . 1 1 38 38 LYS HB3 H 1 2.04 . . 2 . . . . . . . . 2959 1 4 . 1 1 38 38 LYS HG2 H 1 1.33 . . 1 . . . . . . . . 2959 1 5 . 1 1 38 38 LYS HG3 H 1 1.33 . . 1 . . . . . . . . 2959 1 6 . 1 1 38 38 LYS HD2 H 1 1.73 . . 1 . . . . . . . . 2959 1 7 . 1 1 38 38 LYS HD3 H 1 1.73 . . 1 . . . . . . . . 2959 1 8 . 1 1 38 38 LYS HE2 H 1 2.94 . . 1 . . . . . . . . 2959 1 9 . 1 1 38 38 LYS HE3 H 1 2.94 . . 1 . . . . . . . . 2959 1 stop_ save_